CARMILs (Capping protein Arp2/3 Myosin I Linker) are 1000 residue, multi-domain scaffold proteins expressed from protozoa to man that have been studied extensively with regard to their ability to bind Capping Protein (CP) and reduce its affinity for the actin filament barbed end. CARMIL proteins also appear to play important roles in signal transduction, as they exhibit genetic and physical interactions with the Rac GEF Trio (Liang et al MBoC 2009; Vanderzalm et al. Dev. 2009), and T cells lacking CARMIL-2 exhibit a profound block in signaling downstream of CD28, the major co-receptor for T cell signaling (Liang et al Nat. Immunol. 2013). In previous work (Jung et al JCB 2001), we showed that Dictyostelium CARMIL binds CP, the Arp2/3 complex and myosin I (through its SH3 domain), and it is required for actin-dependent processes such as chemotaxis and micropinocytosis to be robust. Here we describe studies of CARMIL-GAP, a second Dictyostelium CARMIL that contains, in addition to all the normal CARMIL domains (including the CP binding CPI domain), a 130 residue insertion that, by homology, is a GTPase activating (GAP) domain for Rho-GTPases. This domain probably possesses GAP activity given that full length CARMIL-GAP can only be over-expressed in cells if this domain contains a point mutation (R737A) that blocks GAP activity in all characterized GAP proteins. Like CARMIL, CARMIL-GAP localizes to actin-rich structures and is expressed in both vegetative and starved, developing cells. Consistently, CARMIL-GAP null cell lines created by homologous recombination exhibit pronounced defects in several actin-based processes, including phagocytosis, motility and chemotactic aggregation. Importantly, expression of GFP-FL CARMIL-GAP in CARMIL-GAP null cells rescues the defects in phagocytosis and chemotactic aggregation. Mass spec analyses of pull downs made using the GAP domain indicate that CARMIL-GAP binds Rac 1a, one of eleven Rac isoforms expressed in Dictyostelium. Current efforts are directed at demonstrating regulation of Rac 1a by CARMIL-GAP in vivo, and at identifying which domains within CARMIL-GAP (e.g. the GAP domain, the CPI domain) are most critical for its function.